High-resolution proton magnetic resonance study of porcine colipase and its interactions with taurodeoxycholate.

A high-resolution 270-MHz proton NMR study of procine colipase I has been performed, and the resonances in the aromatic region of the spectrum have been assigned to amino acid residues by pH titration and decoupling experiments. The apparent pKa values of the three tyrosines were calculated to be 10.2, 10.3, and 11.8 with one of the tyrosines having properties of a "buried" residue. A tentative assignment to the amino acid residues in the primary seuqence of colipase will be discussed. The effects of taurodeoxycholate (TDC) and a positively charged deoxycholate derivative on the aromatic region of the colipase NMR spectrum indicate that all tyrosines and one histidine are affected by the bile-salt binding, suggesting that the TDC molecules bind near these residues to a hydrophobic region on colipase. Measurements and calculations on the line width of the C(18) methyl group resonance suggest that the line-width increase of this resonance upon interaction of TDC with colipase to a large extent can be explained as due to the slower tumbling of the TDC molecules bound to colipase.